Binding sites and hydrophobic pockets in Human Thioredoxin 1 determined by normal mode analysis.
J Struct Biol
; 184(2): 293-300, 2013 Nov.
Article
en En
| MEDLINE
| ID: mdl-24036282
ABSTRACT
The Thioredoxin (Trx) system plays important roles in several diseases (e.g. cancer, viral infections, cardiovascular and neurodegenerative diseases). Therefore, there is a therapeutic interest in the design of modulators of this system. In this work, we used normal mode analysis to identify putative binding site regions for Human Trx1 that arise from global motions. We identified three possible inhibitor's binding regions that corroborate previous experimental findings. We show that intrinsic motions of the protein are related to the exposure of hydrophobic regions and non-active site cysteines that could constitute new binding sites for inhibitors.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Asunto principal:
Tiorredoxinas
Tipo de estudio:
Prognostic_studies
Límite:
Humans
Idioma:
En
Revista:
J Struct Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2013
Tipo del documento:
Article
País de afiliación:
Brasil